› 1uxr

X-ray diffraction
2.3Å resolution

Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) from Thermoproteus tenax

Released:
DOI: 10.2210/pdb1uxr/pdb
PDB entry 1uxr coloured by chain, front view.
PDB entry 1uxr coloured by chain, side view.
PDB entry 1uxr coloured by chain, top view.
Source organism: Thermoproteus tenax
Primary publication:
Structural Basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-Phosphate dehydrogenase from Thermoproteus tenax.
Lorentzen E, Hensel R, Knura T, Ahmed H, Pohl E
J Mol Biol 341 815-28 (2004)
PMID: 15288789

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate + NAD(P)(+) + H(2)O = 3-phospho-D-glycerate + NAD(P)H
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129594 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 501 amino acids
Theoretical weight: 54.22 KDa
Source organism: Thermoproteus tenax
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O57693 (Residues: 1-501; Coverage: 100%)
Gene name: gapN
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
2 bound ligands:
Ligand F6P 1 x F6P
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P6222
Unit cell:
a: 185.35Å b: 185.35Å c: 134.56Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.21 0.227
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
5 more

2 mentions without citation

Exploiting protein flexibility to predict the location of allosteric sites.
Panjkovich et al. (2012)
1 more